Comparison of chromatographic ion-exchange resins: III. Strong cation-exchange resins
A comparative study was performed on strong cation-exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and SEM pictures of chromatographic resins. The resins tested included: SP Sepharose XL, Poros 50 HS, Toyopearl SP 55...
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| Veröffentlicht in: | Journal of Chromatography A 2004-04, Vol.1034 (1), p.85-97 |
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| container_title | Journal of Chromatography A |
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| creator | Staby, Arne Sand, Maj-Britt Hansen, Ronni G. Jacobsen, Jan H. Andersen, Line A. Gerstenberg, Michael Bruus, Ulla K. Jensen, Inge Holm |
| description | A comparative study was performed on strong cation-exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and SEM pictures of chromatographic resins. The resins tested included: SP Sepharose XL, Poros 50 HS, Toyopearl SP 550c, SP Sepharose BB, Source 30S, TSKGel SP-5PW-HR20, and Toyopearl SP 650c. Testing was performed with four different proteins: anti-FVII Mab (IgG), aprotinin, lysozyme, and myoglobin. Dependence of pH on retention was generally very low for proteins with high pI. An unexpected binding at pH 7.5 of anti-FVII Mab with pI |
| doi_str_mv | 10.1016/j.chroma.2004.01.026 |
| format | Article |
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Strong cation-exchange resins</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Staby, Arne ; Sand, Maj-Britt ; Hansen, Ronni G. ; Jacobsen, Jan H. ; Andersen, Line A. ; Gerstenberg, Michael ; Bruus, Ulla K. ; Jensen, Inge Holm</creator><creatorcontrib>Staby, Arne ; Sand, Maj-Britt ; Hansen, Ronni G. ; Jacobsen, Jan H. ; Andersen, Line A. ; Gerstenberg, Michael ; Bruus, Ulla K. ; Jensen, Inge Holm</creatorcontrib><description>A comparative study was performed on strong cation-exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and SEM pictures of chromatographic resins. The resins tested included: SP Sepharose XL, Poros 50 HS, Toyopearl SP 550c, SP Sepharose BB, Source 30S, TSKGel SP-5PW-HR20, and Toyopearl SP 650c. Testing was performed with four different proteins: anti-FVII Mab (IgG), aprotinin, lysozyme, and myoglobin. Dependence of pH on retention was generally very low for proteins with high pI. An unexpected binding at pH 7.5 of anti-FVII Mab with pI<7.5 was observed on several resins. Efficiency results show the expected trend of higher dependence of the plate height with increasing flow rate of soft resins compared to resins for medium and high-pressure operation. Determination of particle size distribution by two independent methods, Coulter counting and SEM, was in very good agreement. The mono-dispersed nature of Source 30S was confirmed. Binding to cation-exchange resins as a function of ionic strength varies depending on the specific protein. Generally, binding and elution at high salt concentration may be performed with Toyopearl SP 550c and Poros 50 HS, while binding and elution at low salt concentration may be performed with Toyopearl SP 650c. A very high binding capacity was obtained with SP Sepharose XL. Comparison of static capacity and dynamic capacity at 10% break-through shows in general approximately 50–80% utilisation of the total available capacity during chromatographic operation. A general good agreement was obtained between this study and data obtained by others. The results of this study may be used for selection of resins for testing in process development. The validity of experiments and results with model proteins were tested using human insulin precursor in pure state and in real feed-stock on Toyopearl SP 550c, SP Sepharose BB, and Toyopearl SP 650c. Results showed good agreement with experiments with model proteins.</description><identifier>ISSN: 0021-9673</identifier><identifier>DOI: 10.1016/j.chroma.2004.01.026</identifier><identifier>PMID: 15116917</identifier><identifier>CODEN: JOCRAM</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Analysis ; Analytical biochemistry: general aspects, technics, instrumentation ; Analytical chemistry ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Cation Exchange Resins ; Chemistry ; Chromatographic methods and physical methods associated with chromatography ; Dynamic capacity ; Exact sciences and technology ; Fundamental and applied biological sciences. Psychology ; General pharmacology ; Hydrogen-Ion Concentration ; Ion-exchangers ; Medical sciences ; Microscopy, Electron, Scanning ; Particle Size ; Pharmacology. Drug treatments ; Proteins ; Static capacity ; Stationary phases, LC</subject><ispartof>Journal of Chromatography A, 2004-04, Vol.1034 (1), p.85-97</ispartof><rights>2004 Elsevier B.V.</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.chroma.2004.01.026$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15611482$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15116917$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Staby, Arne</creatorcontrib><creatorcontrib>Sand, Maj-Britt</creatorcontrib><creatorcontrib>Hansen, Ronni G.</creatorcontrib><creatorcontrib>Jacobsen, Jan H.</creatorcontrib><creatorcontrib>Andersen, Line A.</creatorcontrib><creatorcontrib>Gerstenberg, Michael</creatorcontrib><creatorcontrib>Bruus, Ulla K.</creatorcontrib><creatorcontrib>Jensen, Inge Holm</creatorcontrib><title>Comparison of chromatographic ion-exchange resins: III. Strong cation-exchange resins</title><title>Journal of Chromatography A</title><addtitle>J Chromatogr A</addtitle><description>A comparative study was performed on strong cation-exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and SEM pictures of chromatographic resins. The resins tested included: SP Sepharose XL, Poros 50 HS, Toyopearl SP 550c, SP Sepharose BB, Source 30S, TSKGel SP-5PW-HR20, and Toyopearl SP 650c. Testing was performed with four different proteins: anti-FVII Mab (IgG), aprotinin, lysozyme, and myoglobin. Dependence of pH on retention was generally very low for proteins with high pI. An unexpected binding at pH 7.5 of anti-FVII Mab with pI<7.5 was observed on several resins. Efficiency results show the expected trend of higher dependence of the plate height with increasing flow rate of soft resins compared to resins for medium and high-pressure operation. Determination of particle size distribution by two independent methods, Coulter counting and SEM, was in very good agreement. The mono-dispersed nature of Source 30S was confirmed. Binding to cation-exchange resins as a function of ionic strength varies depending on the specific protein. Generally, binding and elution at high salt concentration may be performed with Toyopearl SP 550c and Poros 50 HS, while binding and elution at low salt concentration may be performed with Toyopearl SP 650c. A very high binding capacity was obtained with SP Sepharose XL. Comparison of static capacity and dynamic capacity at 10% break-through shows in general approximately 50–80% utilisation of the total available capacity during chromatographic operation. A general good agreement was obtained between this study and data obtained by others. The results of this study may be used for selection of resins for testing in process development. The validity of experiments and results with model proteins were tested using human insulin precursor in pure state and in real feed-stock on Toyopearl SP 550c, SP Sepharose BB, and Toyopearl SP 650c. Results showed good agreement with experiments with model proteins.</description><subject>Analysis</subject><subject>Analytical biochemistry: general aspects, technics, instrumentation</subject><subject>Analytical chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cation Exchange Resins</subject><subject>Chemistry</subject><subject>Chromatographic methods and physical methods associated with chromatography</subject><subject>Dynamic capacity</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ion-exchangers</subject><subject>Medical sciences</subject><subject>Microscopy, Electron, Scanning</subject><subject>Particle Size</subject><subject>Pharmacology. Drug treatments</subject><subject>Proteins</subject><subject>Static capacity</subject><subject>Stationary phases, LC</subject><issn>0021-9673</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0T1PwzAQBmAPIAqFf4BQFtgSfE5iJwxIqOIjUiUG6Gw5ttO6Suxgpwj-PalSJAamu-HRK929CF0CTgADvd0mcuNdJxKCcZZgSDChR-gUYwJxSVk6Q2chbDEGhhk5QTPIAWgJ7BStFq7rhTfB2cg10RQzuLUX_cbIyDgb6y-5EXatI6-DseEuqqoqid4G7-w6kmL4x5yj40a0QV8c5hytnh7fFy_x8vW5WjwsY01KMsQp5KVilGqSZoTVddaUOFeZFIKWpSCM1IQW9bgwpiQVqkmpIo1mWVGQJi_ydI5uptzeu4-dDgPvTJC6bYXVbhc4g4LlZU5GeHWAu7rTivfedMJ_899HjOD6AESQom28sNKEP44CZMU-6H5yejzr02jPgzTaSq2M13LgyhkOmO9b4Vs-vZPvW-EY-NhK-gOz8IHN</recordid><startdate>20040423</startdate><enddate>20040423</enddate><creator>Staby, Arne</creator><creator>Sand, Maj-Britt</creator><creator>Hansen, Ronni G.</creator><creator>Jacobsen, Jan H.</creator><creator>Andersen, Line A.</creator><creator>Gerstenberg, Michael</creator><creator>Bruus, Ulla K.</creator><creator>Jensen, Inge Holm</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20040423</creationdate><title>Comparison of chromatographic ion-exchange resins: III. Strong cation-exchange resins</title><author>Staby, Arne ; Sand, Maj-Britt ; Hansen, Ronni G. ; Jacobsen, Jan H. ; Andersen, Line A. ; Gerstenberg, Michael ; Bruus, Ulla K. ; Jensen, Inge Holm</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e292t-3159d766e23427bb4f905d4caa699a272b268ba2777dc6adf36d2fe74882f5853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Analysis</topic><topic>Analytical biochemistry: general aspects, technics, instrumentation</topic><topic>Analytical chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cation Exchange Resins</topic><topic>Chemistry</topic><topic>Chromatographic methods and physical methods associated with chromatography</topic><topic>Dynamic capacity</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Ion-exchangers</topic><topic>Medical sciences</topic><topic>Microscopy, Electron, Scanning</topic><topic>Particle Size</topic><topic>Pharmacology. Drug treatments</topic><topic>Proteins</topic><topic>Static capacity</topic><topic>Stationary phases, LC</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Staby, Arne</creatorcontrib><creatorcontrib>Sand, Maj-Britt</creatorcontrib><creatorcontrib>Hansen, Ronni G.</creatorcontrib><creatorcontrib>Jacobsen, Jan H.</creatorcontrib><creatorcontrib>Andersen, Line A.</creatorcontrib><creatorcontrib>Gerstenberg, Michael</creatorcontrib><creatorcontrib>Bruus, Ulla K.</creatorcontrib><creatorcontrib>Jensen, Inge Holm</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of Chromatography A</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Staby, Arne</au><au>Sand, Maj-Britt</au><au>Hansen, Ronni G.</au><au>Jacobsen, Jan H.</au><au>Andersen, Line A.</au><au>Gerstenberg, Michael</au><au>Bruus, Ulla K.</au><au>Jensen, Inge Holm</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparison of chromatographic ion-exchange resins: III. Strong cation-exchange resins</atitle><jtitle>Journal of Chromatography A</jtitle><addtitle>J Chromatogr A</addtitle><date>2004-04-23</date><risdate>2004</risdate><volume>1034</volume><issue>1</issue><spage>85</spage><epage>97</epage><pages>85-97</pages><issn>0021-9673</issn><coden>JOCRAM</coden><abstract>A comparative study was performed on strong cation-exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and SEM pictures of chromatographic resins. The resins tested included: SP Sepharose XL, Poros 50 HS, Toyopearl SP 550c, SP Sepharose BB, Source 30S, TSKGel SP-5PW-HR20, and Toyopearl SP 650c. Testing was performed with four different proteins: anti-FVII Mab (IgG), aprotinin, lysozyme, and myoglobin. Dependence of pH on retention was generally very low for proteins with high pI. An unexpected binding at pH 7.5 of anti-FVII Mab with pI<7.5 was observed on several resins. Efficiency results show the expected trend of higher dependence of the plate height with increasing flow rate of soft resins compared to resins for medium and high-pressure operation. Determination of particle size distribution by two independent methods, Coulter counting and SEM, was in very good agreement. The mono-dispersed nature of Source 30S was confirmed. Binding to cation-exchange resins as a function of ionic strength varies depending on the specific protein. Generally, binding and elution at high salt concentration may be performed with Toyopearl SP 550c and Poros 50 HS, while binding and elution at low salt concentration may be performed with Toyopearl SP 650c. A very high binding capacity was obtained with SP Sepharose XL. Comparison of static capacity and dynamic capacity at 10% break-through shows in general approximately 50–80% utilisation of the total available capacity during chromatographic operation. A general good agreement was obtained between this study and data obtained by others. The results of this study may be used for selection of resins for testing in process development. The validity of experiments and results with model proteins were tested using human insulin precursor in pure state and in real feed-stock on Toyopearl SP 550c, SP Sepharose BB, and Toyopearl SP 650c. Results showed good agreement with experiments with model proteins.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>15116917</pmid><doi>10.1016/j.chroma.2004.01.026</doi><tpages>13</tpages></addata></record> |
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| subjects | Analysis Analytical biochemistry: general aspects, technics, instrumentation Analytical chemistry Analytical, structural and metabolic biochemistry Biological and medical sciences Cation Exchange Resins Chemistry Chromatographic methods and physical methods associated with chromatography Dynamic capacity Exact sciences and technology Fundamental and applied biological sciences. Psychology General pharmacology Hydrogen-Ion Concentration Ion-exchangers Medical sciences Microscopy, Electron, Scanning Particle Size Pharmacology. Drug treatments Proteins Static capacity Stationary phases, LC |
| title | Comparison of chromatographic ion-exchange resins: III. Strong cation-exchange resins |
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